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- W4220762287 abstract "Abrupt aggregation of misfolded proteins is a hallmark of a large number of severe pathologies, including diabetes types 1 and 2, Alzheimer, and Parkinson diseases. A growing body of evidence suggests that lipids can uniquely change rates of amyloid-associated proteins as well as modify the structure of formed oligomers and fibrils. In this study, we utilize atomic force microscopy infrared (AFM-IR) spectroscopy, also known as nano-IR spectroscopy, to examine the structure of individual insulin oligomers, protofilaments, and fibrils grown in the presence of phospholipids. Our findings show that AFM-IR spectra of insulin oligomers have strong signals of C-H and PO2- vibrations, which points on the presence of lipids in the oligomer structure. Furthermore, substantial shifts in lipid vibrations in AFM-IR spectra of the oligomers relative to the corresponding bands of pure lipids have been observed. This points on strong interactions between a lipid and a protein that are developed at the stage of the oligomer formation." @default.
- W4220762287 created "2022-04-03" @default.
- W4220762287 creator A5015591767 @default.
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- W4220762287 date "2022-03-10" @default.
- W4220762287 modified "2023-10-18" @default.
- W4220762287 title "Nanoscale Structural Analysis of a Lipid-Driven Aggregation of Insulin" @default.
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- W4220762287 doi "https://doi.org/10.1021/acs.jpclett.1c04012" @default.
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